Tandem pore domain potassium channel

The two-pore-domain potassium channel (not to be confused with the small family of two-pore channels) a family of 15 members form what is known as "leak channels" which possess Goldman-Hodgkin-Katz (open) rectification.^[1] These channels are regulated by several mechanisms including oxygen tension, pH, mechanical stretch, and G-proteins . Their name is derived from the fact that the α subunits consist of four transmembrane segments, each containing two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane.

Below is a list of the 15 known two-pore-domain human potassium channels:^[1]

Gene	Channel^[2]	Family	Aliases
KCNK1	K_2p1.1	TWIK^[3]^[4]	TWIK-1
KCNK2	K_2p2.1	TREK^[3]^[4]	TREK-1
KCNK3	K_2p3.1	TASK^[3]^[4]	TASK-1
KCNK4	K_2p4.1	TREK^[3]^[4]	TRAAK^[5]
KCNK5	K_2p5.1	TASK^[3]^[4]	TASK-2^[6]
KCNK6	K_2p6.1	TWIK^[3]^[4]	TWIK-2
KCNK7	K_2p7.1	TWIK^[3]^[4]
KCNK9	K_2p9.1	TASK^[3]^[4]	TASK-3
KCNK10	K_2p10.1	TREK^[3]^[4]	TREK-2
KCNK12	K_2p12.1	THIK	THIK-2
KCNK13	K_2p13.1	THIK	THIK-1
KCNK15	K_2p15.1	TASK^[3]^[4]	TASK-5
KCNK16	K_2p16.1	TALK^[3]^[4]	TALK-1
KCNK17	K_2p17.1	TALK^[3]^[4]	TALK-2, TASK-4
KCNK18	K_2p18.1		TRIK, TRESK^[3]^[4]^[7]^[8]

References

1 2 Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (Dec 2005). "International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels". Pharmacological Reviews 57 (4): 527–40. doi:10.1124/pr.57.4.12. PMID 16382106.
↑ Gutman GA, Chandy KG, Adelman JP, Aiyar J, Bayliss DA, Clapham DE, et al. (Dec 2003). "International Union of Pharmacology. XLI. Compendium of voltage-gated ion channels: potassium channels". Pharmacological Reviews 55 (4): 583–6. doi:10.1124/pr.55.4.9. PMID 14657415.
1 2 3 4 5 6 7 8 9 10 11 12 13 Enyedi P, Czirják G (Apr 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels". Physiological Reviews 90 (2): 559–605. doi:10.1152/physrev.00029.2009. PMID 20393194.
1 2 3 4 5 6 7 8 9 10 11 12 13 Lotshaw DP (2007). "Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels". Cell Biochemistry and Biophysics 47 (2): 209–56. doi:10.1007/s12013-007-0007-8. PMID 17652773.
↑ Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M (Jun 1998). "A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids". The EMBO Journal 17 (12): 3297–308. doi:10.1093/emboj/17.12.3297. PMC 1170668. PMID 9628867.
↑ Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (Mar 2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nature Reviews. Neuroscience 2 (3): 175–84. doi:10.1038/35058574. PMID 11256078.
↑ Sano Y, Inamura K, Miyake A, Mochizuki S, Kitada C, Yokoi H, Nozawa K, Okada H, Matsushime H, Furuichi K (Jul 2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord". The Journal of Biological Chemistry 278 (30): 27406–12. doi:10.1074/jbc.M206810200. PMID 12754259.
↑ Czirják G, Tóth ZE, Enyedi P (Apr 2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin". The Journal of Biological Chemistry 279 (18): 18550–8. doi:10.1074/jbc.M312229200. PMID 14981085.

External links

Tandem Pore Domain Potassium Channel at the US National Library of Medicine Medical Subject Headings (MeSH)
"Two-P Potassium Channels". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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Tandem pore domain potassium channel

See also

References

External links